Detects human CCL4/MIP-1 beta in ELISAs and Western blots. In sandwich immunoassays, less than 1% cross-reactivity with recombinant human (rh) MIP‑1 alpha is observed and less than 0.1% cross-reactivity with recombinant viral (rv) MIP-I, rvMIP-II, rhMIP‑1δ, recombinant mouse (rm) MIP‑1 alpha, rmMIP‑1 beta, rmMIP-1 gamma, rhGRO beta, rhGRO gamma, rhMCP-1, and rhRANTES is observed.
Polyclonal Goat IgG
S. frugiperda insect ovarian cell line Sf 21-derived recombinant human CCL4/MIP-1 beta
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
CCL4/MIP‑1 beta in Human PBMCs.
CCL4/MIP‑1 beta was detected in immersion fixed human peripheral blood mononuclear cells (PBMCs) using Human CCL4/MIP‑1 beta Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF271) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Streptavidin (red; Catalog # NL999) and counterstained with DAPI (blue). View our protocol for Fluorescent ICC Staining of Non-adherent Cells.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: CCL4/MIP-1 beta
CCL4, also known as macrophage inflammatory protein 1 beta (MIP-1 beta ) is a 7.8 kDa beta chemokine that is secreted at sites of inflammation by activated leukocytes, lymphocytes, vascular endothelial cells, and pulmonary smooth muscle cells. CCL4 attracts a variety of immune cells to sites of microbial infection as well as to other pathologic inflammation such as allergic asthma and ischemic myocardium. A CCL4 deficiency in mice promotes the development of autoantibodies, possibly as a result of compromised regulatory T cell recruitment. CCL4 is secreted from activated monocytes as a heterodimer with CCL3/MIP-1 alpha. The first two N-terminal amino acids can be cleaved from human CCL4 by CD26/DPPIV. Both the full length and truncated forms exert biological activity through CCR5, and the truncated form additionally interacts with CCR1 and CCR2b. In humans, the ability of CCL4 to bind CCR5 inhibits the cellular entry of M-tropic HIV-1 which utilizes CCR5 as a coreceptor. Both forms of CCL4 block HIV-1 infection of T cells by inducing the downregulation of CCR5. Mature human CCL4 shares 77% and 80% aa sequence identity with mouse and rat CCL4, respectively.
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